Glycine metabolism in anaerobes

Andreesen, Jan R.

doi:10.1007/bf00871641

Cited by 102 publications

(88 citation statements)

References 149 publications

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“…This complex acts in consort with thioredoxin and thioredoxin reductase to deaminate and phosphorylate the substrate, thus contributing to the pool of phosphorylated compounds (44). Alternate substrates in Clostridium and Eubacterium species include betaine, sarcosine, and N-methyl derivatives of glycine; the polypeptide subunits derived from the multiple grdB and grdE genes in T. denticola may affect substrate specificity and permit the utilization of amino acids and other compounds for substrate phosphorylation and ATP production.…”

Section: Resultsmentioning

confidence: 99%

Comparison of the genome of the oral pathogen Treponema denticola with other spirochete genomes

Seshadri

Myers

Tettelin

et al. 2004

Proc. Natl. Acad. Sci. U.S.A.

253

314

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We present the complete 2,843,201-bp genome sequence of Treponema denticola (ATCC 35405) an oral spirochete associated with periodontal disease. Analysis of the T. denticola genome reveals factors mediating coaggregation, cell signaling, stress protection, and other competitive and cooperative measures, consistent with its pathogenic nature and lifestyle within the mixed-species environment of subgingival dental plaque. Comparisons with previously sequenced spirochete genomes revealed specific factors contributing to differences and similarities in spirochete physiology as well as pathogenic potential. The T. denticola genome is considerably larger in size than the genome of the related syphiliscausing spirochete Treponema pallidum. The differences in gene content appear to be attributable to a combination of three phenomena: genome reduction, lineage-specific expansions, and horizontal gene transfer. Genes lost due to reductive evolution appear to be largely involved in metabolism and transport, whereas some of the genes that have arisen due to lineage-specific expansions are implicated in various pathogenic interactions, and genes acquired via horizontal gene transfer are largely phagerelated or of unknown function.

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Section: Resultsmentioning

confidence: 99%

Comparison of the genome of the oral pathogen Treponema denticola with other spirochete genomes

Seshadri

Myers

Tettelin

et al. 2004

Proc. Natl. Acad. Sci. U.S.A.

253

314

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“…Anaerobically, catabolic pathways containing GB reductase cleave GB to acetate and trimethylamine (TMA) as excreted products. GB reduction is often considered the sole fate of the compound under anaerobic conditions (17)(18)(19). However, there have been sporadic reports in the literature that GB reduction is not the only route of microbial GB catabolism under anoxic conditions.…”

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confidence: 99%

A nonpyrrolysine member of the widely distributed trimethylamine methyltransferase family is a glycine betaine methyltransferase

Ticak

Kountz²,

Girosky³

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

157

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Significance Pyrrolysine, the 22nd amino acid, is found in few proteins. One, the trimethylamine methyltransferase MttB, forms a small portion of a large family of proteins. Most in this family lack pyrrolysine and have no known activity. We show that one such protein, MtgB, is a glycine betaine methyltransferase, providing functional context that may explain the relationship between family members with and without pyrrolysine. Close relatives of MtgB are encoded in many of the abundant bacteria in the oceans, as well as different microbes undertaking symbioses ranging from plants to humans. This finding implies that MtgB might partake in a widespread and underappreciated pathway of GB metabolism contributing significantly to global carbon and nitrogen cycling as well as human health.

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“…A similar reaction is catalyzed by glycine reductase, which cleaves glycine to acetyl phosphate and ammonia (7,8). Different reaction mechanisms were postulated for the catalytic cascades of these enzymes (2,3,7,9). D-Proline is first activated by an enzyme-bound pyruvoyl group.…”

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confidence: 99%

Identification of d-Proline Reductase fromClostridium sticklandiias a Selenoenzyme and Indications for a Catalytically Active Pyruvoyl Group Derived from a Cysteine Residue by Cleavage of a Proprotein

Kabisch

Gräntzdörffer

Schierhorn

et al. 1999

Journal of Biological Chemistry

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Highly active D-proline reductase was obtained from Clostridium sticklandii by a modified purification scheme. The cytoplasmic enzyme had a molecular mass of about 870 kDa and was composed of three subunits with molecular masses of 23, 26, and 45 kDa. The 23-kDa subunit contained a carbonyl group at its N terminus, which could either be labeled with fluorescein thiosemicarbazide or removed by o-phenylenediamine; thus, Nterminal sequencing became feasible for this subunit. L-[14 C]proline was covalently bound to the 23-kDa subunit if proline racemase and NaBH 4 were added. Selenocysteine was detected in the 26-kDa subunit, which correlated with an observed selenium content of 10.6 g-atoms in D-proline reductase. No other non-proteinaceous cofactor was identified in the enzyme. A 4.8-kilobase pair (kb) EcoRI fragment was isolated and sequenced containing the two genes prdA and prdB. prdA coding for a 68-kDa protein was most likely translated as a proprotein that was posttranslationally cleaved at a threonine-cysteine site to give the 45-kDa subunit and most probably a pyruvoyl-containing 23-kDa subunit. The gene prdB encoded the 26-kDa subunit and contained an in frame UGA codon for selenocysteine insertion. prdA and prdB were transcribed together on a transcript of 4.5 kb; prdB was additionally transcribed as indicated by a 0.8-kb mRNA species.

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Glycine metabolism in anaerobes

Cited by 102 publications

References 149 publications

Comparison of the genome of the oral pathogen Treponema denticola with other spirochete genomes

Comparison of the genome of the oral pathogen Treponema denticola with other spirochete genomes

A nonpyrrolysine member of the widely distributed trimethylamine methyltransferase family is a glycine betaine methyltransferase

Identification of d-Proline Reductase fromClostridium sticklandiias a Selenoenzyme and Indications for a Catalytically Active Pyruvoyl Group Derived from a Cysteine Residue by Cleavage of a Proprotein

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